カスパーゼ1
- 関
- IL-1 beta-converting enzyme、interleukin-1beta converting enzyme
WordNet
- any of a group of proteases that mediate apoptosis
Wikipedia preview
出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2015/08/17 03:00:57」(JST)
[Wiki en表示]
| Caspase 1, apoptosis-related cysteine peptidase |
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PDB rendering based on 1bmq.
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| Available structures |
| PDB |
Ortholog search: PDBe, RCSB |
| List of PDB id codes |
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1BMQ, 1IBC, 1ICE, 1RWK, 1RWM, 1RWN, 1RWO, 1RWP, 1RWV, 1RWW, 1RWX, 1SC1, 1SC3, 1SC4, 2FQQ, 2H48, 2H4W, 2H4Y, 2H51, 2H54, 2HBQ, 2HBR, 2HBY, 2HBZ, 3D6F, 3D6H, 3D6M, 3E4C, 3NS7
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| Identifiers |
| Symbols |
CASP1 ; ICE; IL1BC; P45 |
| External IDs |
OMIM: 147678 MGI: 96544 HomoloGene: 133272 ChEMBL: 4801 GeneCards: CASP1 Gene |
| EC number |
3.4.22.36 |
| Gene ontology |
| Molecular function |
• endopeptidase activity
• cysteine-type endopeptidase activity
• protein binding
• cysteine-type endopeptidase activator activity involved in apoptotic process
• cysteine-type endopeptidase activity involved in execution phase of apoptosis
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| Cellular component |
• extracellular region
• cytoplasm
• mitochondrion
• cytosol
• IPAF inflammasome complex
• NLRP1 inflammasome complex
• NLRP3 inflammasome complex
• AIM2 inflammasome complex
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| Biological process |
• response to hypoxia
• proteolysis
• apoptotic process
• activation of cysteine-type endopeptidase activity involved in apoptotic process
• signal transduction
• regulation of autophagy
• response to lipopolysaccharide
• interleukin-1 beta production
• response to ATP
• nucleotide-binding domain, leucine rich repeat containing receptor signaling pathway
• positive regulation of I-kappaB kinase/NF-kappaB signaling
• innate immune response
• positive regulation of interleukin-1 alpha secretion
• positive regulation of interleukin-1 beta secretion
• regulation of inflammatory response
• mitochondrial depolarization
• membrane hyperpolarization
• pyroptosis
• cellular response to mechanical stimulus
• cellular response to organic substance
• execution phase of apoptosis
• programmed necrotic cell death
• toxin transport
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| Sources: Amigo / QuickGO |
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| Orthologs |
| Species |
Human |
Mouse |
| Entrez |
834 |
12362 |
| Ensembl |
ENSG00000137752 |
ENSMUSG00000025888 |
| UniProt |
P29466 |
P29452 |
| RefSeq (mRNA) |
NM_001223 |
NM_009807 |
| RefSeq (protein) |
NP_001214 |
NP_033937 |
| Location (UCSC) |
Chr 11:
105.03 – 105.04 Mb |
Chr 9:
5.3 – 5.31 Mb |
| PubMed search |
[1] |
[2] |
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Caspase 1/Interleukin-1 converting enzyme is an enzyme that proteolytically cleaves other proteins, such as the precursor forms of the inflammatory cytokines interleukin 1β and interleukin 18, into active mature peptides.[1][2][3]
Contents
- 1 Structure
- 2 Function
- 3 Interactions
- 4 See also
- 5 References
- 6 External links
Structure
Caspase 1 is produced as a zymogen that is cleaved into 20 kDa (p20) and 10 kDa (p10) subunits that become part of the active enzyme. Active caspase 1 contains two heterodimers of p20 and p10. It interacts with another CARD domain containing protein called PYCARD (or ASC) and is involved in inflammasome formation and activation of inflammatory processes.[4]
Function
Caspase 1 has been shown to induce cell necrosis or pyroptosis and may function in various developmental stages. Studies of a similar protein in mouse suggest a role in the pathogenesis of Huntington's disease. Alternative splicing of the gene results in five transcript variants encoding distinct isoforms.[5] Recent studies implicated caspase 1 in promoting CD4 T-cell death and inflammation by HIV, two signature events that fuel HIV disease progression to AIDS.[6][7]
Interactions
Caspase 1 has been shown to interact with NLRC4.[8][9]
See also
- The Proteolysis Map
- Caspase
References
- ^ Thornberry NA, Bull HG, Calaycay JR, Chapman KT, Howard AD, Kostura MJ, Miller DK, Molineaux SM, Weidner JR, Aunins J (1992). "A novel heterodimeric cysteine protease is required for interleukin-1 beta processing in monocytes". Nature 356 (6372): 768–74. doi:10.1038/356768a0. PMID 1574116.
- ^ Cerretti DP, Kozlosky CJ, Mosley B, Nelson N, Van Ness K, Greenstreet TA, March CJ, Kronheim SR, Druck T, Cannizzaro LA (1992). "Molecular cloning of the interleukin-1 beta converting enzyme". Science 256 (5053): 97–100. doi:10.1126/science.1373520. PMID 1373520.
- ^ Black RA, Kronheim SR, Merriam JE, March CJ, Hopp TP (1989). "A pre-aspartate-specific protease from human leukocytes that cleaves pro-interleukin-1 beta". J. Biol. Chem. 264 (10): 5323–6. PMID 2784432.
- ^ Mariathasan S, Newton K, Monack DM, Vucic D, French DM, Lee WP, Roose-Girma M, Erickson S, Dixit VM (2004). "Differential activation of the inflammasome by caspase-1 adaptors ASC and Ipaf". Nature 430 (6996): 213–8. doi:10.1038/nature02664. PMID 15190255.
- ^ "Entrez Gene: CASP1 caspase 1, apoptosis-related cysteine peptidase (interleukin 1, beta, convertase)".
- ^ Doitsh G, Galloway NL, Geng X, Yang Z, Monroe KM, Zepeda O, Hunt PW, Hatano H, Sowinski S, Muñoz-Arias I, Greene WC (2014). "Cell death by pyroptosis drives CD4 T-cell depletion in HIV-1 infection". Nature 505 (7484): 509–14. doi:10.1038/nature12940. PMC 4047036. PMID 24356306.
- ^ Monroe KM, Yang Z, Johnson JR, Geng X, Doitsh G, Krogan NJ, Greene WC (2014). "IFI16 DNA sensor is required for death of lymphoid CD4 T cells abortively infected with HIV". Science 343 (6169): 428–32. doi:10.1126/science.1243640. PMC 3976200. PMID 24356113.
- ^ Damiano JS, Oliveira V, Welsh K, Reed JC (2004). "Heterotypic interactions among NACHT domains: implications for regulation of innate immune responses". Biochem. J. 381 (Pt 1): 213–9. doi:10.1042/BJ20031506. PMC 1133779. PMID 15107016.
- ^ Damiano JS, Stehlik C, Pio F, Godzik A, Reed JC (2001). "CLAN, a novel human CED-4-like gene". Genomics 75 (1-3): 77–83. doi:10.1006/geno.2001.6579. PMID 11472070.
External links
- The MEROPS online database for peptidases and their inhibitors: C14.001
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PDB gallery
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1bmq: CRYSTAL STRUCTURE OF THE COMPLEX OF INTERLEUKIN-1BETA CONVERTING ENZYME (ICE) WITH A PEPTIDE BASED INHIBITOR, (3S )-N-METHANESULFONYL-3-({1-[N-(2-NAPHTOYL)-L-VALYL]-L-PROLYL }AMINO)-4-OXOBUTANAMIDE
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1ibc: CRYSTAL STRUCTURE OF INHIBITED INTERLEUKIN-1BETA CONVERTING ENZYME
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1ice: STRUCTURE AND MECHANISM OF INTERLEUKIN-1BETA CONVERTING ENZYME
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1rwk: Crystal structure of human caspase-1 in complex with 3-(2-mercapto-acetylamino)-4-oxo-pentanoic acid
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1rwm: Crystal structure of human caspase-1 in complex with 4-oxo-3-[2-(5-{[4-(quinoxalin-2-ylamino)-benzoylamino]-methyl}-thiophen-2-yl)-acetylamino]-pentanoic acid
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1rwn: Crystal structure of human caspase-1 in complex with 3-{2-ethyl-6-[4-(quinoxalin-2-ylamino)-benzoylamino]-hexanoylamino}-4-oxo-butyric acid
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1rwo: Crystal structure of human caspase-1 in complex with 4-oxo-3-{6-[4-(quinoxalin-2-ylamino)-benzoylamino]-2-thiophen-2-yl-hexanoylamino}-pentanoic acid
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1rwp: Crystal structure of human caspase-1 in complex with 3-{6-[(8-hydroxy-quinoline-2-carbonyl)-amino]-2-thiophen-2-yl-hexanoylamino}-4-oxo-butyric acid
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1rwv: Crystal structure of human caspase-1 in complex with 5-[5-(1-carboxymethyl-2-oxo-propylcarbamoyl)-5-phenyl-pentylsulfamoyl]-2-hydroxy-benzoic acid
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1rww: Crystal structure of human caspase-1 in complex with 4-oxo-3-[(6-{[4-(quinoxalin-2-ylamino)-benzoylamino]-methyl}-pyridine-3-carbonyl)-amino]-butyric acid
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1rwx: Crystal structure of human caspase-1 in complex with 4-oxo-3-{6-[4-(quinoxalin-2-yloxy)-benzoylamino]-2-thiophen-2-yl-hexanoylamino}-butyric acid
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1sc1: Crystal structure of an active-site ligand-free form of the human caspase-1 C285A mutant
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1sc3: Crystal structure of the human caspase-1 C285A mutant in complex with malonate
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1sc4: Crystal structure of the human caspase-1 C285A mutant after removal of malonate
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2fqq: Crystal structure of human caspase-1 (Cys285->Ala, Cys362->Ala, Cys364->Ala, Cys397->Ala) in complex with 1-methyl-3-trifluoromethyl-1H-thieno[2,3-c]pyrazole-5-carboxylic acid (2-mercapto-ethyl)-amide
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2h48: Crystal structure of human caspase-1 (Cys362->Ala, Cys364->Ala, Cys397->Ala) in complex with 3-[2-(2-benzyloxycarbonylamino-3-methyl-butyrylamino)-propionylamino]-4-oxo-pentanoic acid (z-VAD-FMK)
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2hbq: Crystal structure of wildtype human caspase-1 in complex with 3-[2-(2-benzyloxycarbonylamino-3-methyl-butyrylamino)-propionylamino]-4-oxo-pentanoic acid (z-VAD-FMK)
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2hbr: Crystal structure of human caspase-1 (Arg286->Ala) in complex with 3-[2-(2-benzyloxycarbonylamino-3-methyl-butyrylamino)-propionylamino]-4-oxo-pentanoic acid (z-VAD-FMK)
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2hby: Crystal structure of human caspase-1 (Glu390->Ala) in complex with 3-[2-(2-benzyloxycarbonylamino-3-methyl-butyrylamino)-propionylamino]-4-oxo-pentanoic acid (z-VAD-FMK)
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2hbz: Crystal structure of human caspase-1 (Arg286->Ala, Glu390->Ala) in complex with 3-[2-(2-benzyloxycarbonylamino-3-methyl-butyrylamino)-propionylamino]-4-oxo-pentanoic acid (z-VAD-FMK)
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Proteases: cysteine proteases (EC 3.4.22)
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| Caspase |
- Caspase 1
- Caspase 2
- Caspase 3
- Caspase 4
- Caspase 5
- Caspase 6
- Caspase 7
- Caspase 8
- Caspase 9
- Caspase 10
- Caspase 12
- Caspase 13
- Caspase 14
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| Fruit-derived |
- Papain
- Ficain
- Bromelain
- Actinidain
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| Calpain |
- CAPN1
- CAPN2
- CAPN3
- CAPN5
- CAPN6
- CAPN7
- CAPN8
- CAPN9
- CAPN10
- CAPN11
- CAPN12
- CAPN13
- CAPN14
- CAPNS1
- CAPNS2
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| Cathepsin |
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| Other |
- Clostripain
- Cancer procoagulant
- Separase
- Autophagin
- Cruzipain
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- Biochemistry overview
- Enzymes overview
- By EC number: 1.1
- 2
- 3
- 4
- 5
- 6
- 7
- 8
- 10
- 11
- 13
- 14
- 15-18
- 2.1
- 3.1
- 4.1
- 5.1
- 6.1-3
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UpToDate Contents
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English Journal
- Activation of inflammasomes in adipose tissue of women with gestational diabetes.
- Lappas M.SourceDepartment of Obstetrics and Gynaecology, University of Melbourne, Victoria, Australia; Mercy Perinatal Research Centre, Mercy Hospital for Women, Heidelberg, Victoria, Australia. Electronic address: mlappas@unimelb.edu.au.
- Molecular and cellular endocrinology.Mol Cell Endocrinol.2014 Jan 25;382(1):74-83. doi: 10.1016/j.mce.2013.09.011. Epub 2013 Sep 17.
- Gestational diabetes mellitus (GDM) is characterised by maternal peripheral insulin resistance, increased inflammation, and increasing levels of circulating free fatty acids (FFAs) and advanced glycation endproducts (AGEs). Caspase-1 is a key component of the inflammasome, which is activated upon ce
- PMID 24055273
- Inhibition of IL-32 and TSLP production through the attenuation of caspase-1 activation in an animal model of allergic rhinitis by Naju Jjok (Polygonum tinctorium).
- Jeong HJ, Oh HA, Lee BJ, Kim HM.SourceBiochip Research Center and Inflammatory Diseases Research Center, Hoseo University, Asan, Chungnam 336-795, Republic of Korea.
- International journal of molecular medicine.Int J Mol Med.2014 Jan;33(1):142-50. doi: 10.3892/ijmm.2013.1548. Epub 2013 Nov 5.
- In this study, we investigated the effects of Naju Jjok (Polygonum tinctorium Lour., NJJ) on interleukin (IL)-32 and thymic stromal lymphopoietin (TSLP) levels associated with allergic rhinitis (AR). Using female BALB/c mice, we created an animal model of ovalbumin (OVA)-induced AR. Prior to the ca
- PMID 24190435
- HIV-1 Induces the First Signal to Activate the NLRP3 Inflammasome in Monocyte-Derived Macrophages.
- Hernandez JC, Latz E, Urcuqui-Inchima S.SourceInfettare, Facultad de Medicina, Universidad Cooperativa de Colombia, Medellin, Colombia.
- Intervirology.Intervirology.2014;57(1):36-42. doi: 10.1159/000353902. Epub 2013 Sep 5.
- Background/Aims: Inflammasomes are multimolecular complexes that regulate caspase-1. They act as sensors for endogenous and exogenous signals, and mediate the processing of pro-IL-1β into its secreted, biologically active form. The NLRP3 inflammasome and IL-1β are particularly interesting because
- PMID 24008203
Japanese Journal
- Terpinen-4-ol inhibits colorectal cancer growth via reactive oxygen species
- Inhibitory effects of local anesthetics on the proteasome and their biological actions
- HIF-1-mediated suppression of mitochondria electron transport chain function confers resistance to lidocaine-induced cell death
Related Pictures
★リンクテーブル★
[★]
- 関
- caspase 1、interleukin-1beta converting enzyme
[★]
- 関
- caspase 1、IL-1 beta-converting enzyme
[★]
- 英
- caspase 1
- 関
- インターロイキン1β変換酵素、IL-1β変換酵素